2B0R
Crystal Structure of Cyclase-Associated Protein from Cryptosporidium parvum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-08-30 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.258, 58.863, 65.810 |
| Unit cell angles | 90.00, 115.47, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.600 |
| Rwork | 0.216 |
| R-free | 0.26690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k8f |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.387 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.560 |
| High resolution limit [Å] | 2.520 | 6.830 | 2.520 |
| Rmerge | 0.046 | 0.021 | 0.538 |
| Number of reflections | 15686 | ||
| Completeness [%] | 98.6 | ||
| Redundancy | 3.3 | 3.1 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 17% PEG 3350, 0.2M diammonium tartrate, vapor diffusion, hanging drop, temperature 291K |
